Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1989-4-20
pubmed:abstractText
Tyrosinase was isolated from cultured melanoma cells using a procedure involving solubilization of the enzyme by means of Triton X-100, followed by different types of chromatography and tryptic digestion to make the enzyme soluble even in the absence of detergent. Starting with a membranous material containing 72 mg protein, 0.21 mg tyrosinase was obtained. The recovery of tyrosinase was 36% of the quantity found in the membranous starting material. In order to acquire a completely purified enzyme preparation suitable for amino acid sequence analysis, SDS-PAGE followed by blotting onto a polyvinylidene difluoride membrane was performed as a final step. The apparent molecular weight was found to be 66,000. Determination of the amino acids of the aminoterminal portion by automated Edman degradation showed the following sequence: His-Phe-Pro-Arg-Ala-X-Val-Ser-Ser-Lys-Asn-Leu-Met-Glu-Lys-Glu-X-X-Pro-Pr o-The enzyme purified has an amino acid sequence identical with that of human tyrosinase deduced from c-DNA by Kwon et al. Striking similarities between our amino acid sequence and that predicted by Yamamoto et al. from mouse tyrosinase c-DNA were also observed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0001-5555
pubmed:author
pubmed:issnType
Print
pubmed:volume
69
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
125-31
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Isolation of human tyrosinase from cultured melanoma cells.
pubmed:affiliation
Department of Pharmacology, University of Lund, Malmö, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't